Separation of a complete set of basic, diastereomeric pentapeptides by reversed-phase ion-pair chromatography.
The resolving power of liquid chromatography systems containing 1-pentane sulfonate, previously used to analyze basic hydrophilic peptides related to substrates of cAMP-dependent protein kinase, has been studied with respect to diastereomeric peptides. A set of peptides comprising RRASV and its five diastereomers containing one D-amino acid were used as model compounds. Complete resolution of all the peptides could be accomplished both with ethanol and acetonitrile as organic modifiers. The separation of the various peptides within the set turned out to be only modestly changed under the conditions investigated. These new results clearly demonstrate the potential of the chromatography systems studied.
Nyasse
B
B
Department of Biochemistry, University of Uppsala, Sweden.
Fransson
B
B
Ragnarsson
U
U
D000595:Amino Acid Sequence; D002853:Chromatography, Liquid / Q000379:methods; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000302:isolation & purification*; D013237:Stereoisomerism
D009842:Oligopeptides